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Faculty Selected Works of Chung Wong
Article
The Structure of Sky1p Reveals a Novel Mechanism for Constitutive Activity
Nature Structural & Molecular Biology (2001)
  • B Nolen, University of California, San Diego
  • C.Y Yun, University of California, San Diego
  • C.F Wong, University of California, San Diego
  • J.A McCammon, University of California, San Diego
  • X.D Fu, University of California, San Diego
  • G. Ghosh, University of California, San Diego
Link
Abstract
Sky1p is the only member of the SR protein kinase (SRPK) family in Saccharomyces cerevisiae. SRPKs are constitutively active kinases that display remarkable substrate specificity and have been implicated in RNA processing. Here we present the three-dimensional structure of a fully active truncated Sky1p. Analysis of the structure and structure-based functional studies reveal that the C-terminal tail, an unusual Glu residue located in the P+1 loop, and a unique mechanism for the positioning of helix alpha C act together to render Sky1p constitutively active. We have modeled a substrate peptide bound to Sky1p. The modeled complex combined with mutagenesis studies illustrate the molecular basis for substrate recognition by this kinase and suggest a mechanism by which SRPKs catalyze a sequential phosphorylation reaction of the consecutive RS dipeptide repeats characteristic of mammalian SRPK substrates.
Disciplines
Publication Date
February 1, 2001
DOI
10.1038/84178
Citation Information
B Nolen, C.Y Yun, C.F Wong, J.A McCammon, et al.. "The Structure of Sky1p Reveals a Novel Mechanism for Constitutive Activity" Nature Structural & Molecular Biology Vol. 8 Iss. 2 (2001) p. 176 - 183
Available at: http://works.bepress.com/chung-wong/44/